Entry
Name
myeloperoxidase;
MPO;
verdoperoxidase
Class
Oxidoreductases;
Acting on a peroxide as acceptor;
Peroxygenases
BRITE hierarchy
Sysname
chloride:hydrogen-peroxide oxidoreductase (hypochlorite-forming)
Reaction(IUBMB)
Cl- + H2O2 + H+ = HClO + H2O [RN:
R09564 ]
Reaction(KEGG)
Substrate
Product
Comment
Contains calcium and covalently bound heme (proximal ligand histidine). It is present in phagosomes of neutrophils and monocytes, where the hypochlorite produced is strongly bactericidal. It differs from EC
1.11.1.10 chloride peroxidase in its preference for formation of hypochlorite over the chlorination of organic substrates under physiological conditions (pH 5-8). Hypochlorite in turn forms a number of antimicrobial products (Cl2, chloramines, hydroxyl radical, singlet oxygen). MPO also oxidizes bromide, iodide and thiocyanate. In the absence of halides, it oxidizes phenols and has a moderate peroxygenase activity toward styrene.
History
EC 1.11.2.2 created 2011
Pathway
ec00983 Drug metabolism - other enzymes
Orthology
Genes
CGE : 100752227(Mpo) 100757792
PLEU : 114699237 114699257
CCAN : 109674413 109702951
PLOP : 125366055 125366110(Mpo)
MDO : 100012330(MPO) 100022606
GAS : 123246127(MPO) 123246781
GGA : 417466(LPO) 417467(MPO)
LMUT : 125703182 125703183
NMEL : 110407540(EPX) 110407753
APLA : 101801315 101805061
ACYG : 106041022 106041024(MPO)
CATA : 118254071 118254112
AFUL : 116497396 116497447
OTC : 121346857(EPX) 121346871
PRUF : 121362958 121362959(EPX)
CBRC : 103618347 103618349
ACHL : 103802301 103802303 103808840
MMEA : 130574635 130574636
HRT : 120761526 120761527(MPO)
FPG : 101914513(EPX) 101914689(MPO)
EGZ : 104131757 104131758(MPO)
PLET : 104628114 104628115
PCAO : 104041373 104049832
ACUN : 113487144 113487180(MPO)
TALA : 104366892 104366894
PADL : 103916612 103916613
AFOR : 103896569 103896570
ACHC : 115347511 115347673
HALD : 104314380 104314381
AGEN : 126039372 126039769
CCRI : 104165474 104167995
CMAC : 104478087 104482911
BREG : 104631223 104635066
GSTE : 104253887 104256813
PGUU : 104466180 104466182(LPO)
ACAR : 104531742 104531743
CPEA : 104391004 104391006(MPO)
CUCA : 104057358 104057361
AAM : 106496096 106496104(MPO)
AROW : 112964994 112965020(MPO)
NPD : 112956708(MPO) 112956744
SCAM : 104146231(MPO) 104146262
CPOO : 109317469 109317472
CMY : 102933916 102934149 102941880
CCAY : 125623878(MPO) 125624086
CPIC : 101935994 101946833 101947097
TST : 117867690(MPO) 117867693 117867698
CABI : 116818731(MPO) 116818741 116818742
MRV : 120387502 120387503 120387580
PBI : 103062626 103062866(LPO)
CTIG : 120309089 120309240(MPO)
TSR : 106549249(MPO) 106553876(LPO)
STOW : 125445776 125446010
XLA : 373710(mpo.S) 394386(mpo.L) 398084(epx.L)
XTR : 100490938(mpo) 100496213(epx)
NPR : 108785838 108785844 108797850
RTEM : 120927532 120927666 120927668 120927671
BBUF : 120993645 120993647 120993648 120994701 120994817
BGAR : 122931700 122931701 122931839 122931840 122932447 122932595 122940269
CCAR : 109052003 109052065
LCM : 102347787 102348047(MPO)
RTP : 109913294 109913296 109926715 109937198 109937200
BCOO : 119072211 119073474 119084658
ESN : 126992742 126999343 126999344
TCF : 131877769 131881259 131881559 131892322 131893385
PVUL : 126814675 126815268 126818155
HRF : 124118159 124122769 124136579 124136580 124141281 124141282 124141286 124141289
HRJ : 124253595 124256926 124262128
CRG : 105319077 105333777 105347615 117683867
CVN : 111099498 111099865 111099927 111101154 111101742 111102226 111114088 111123883
CANU : 128162520 128163610 128181364 128192858
OED : 125665352 125682350 125682351
PMAX : 117340028 117342135
MMER : 123537740 123538598 123539213 123541376 123546341
RPHI : 132724008 132725507 132727046 132729624 132735490 132739235 132741246
DPOL : 127845366 127845367 127847020 127848042 127849115 127849117 127849118 127860390 127863206 127866032 127873828 127878283 127879920
» show all
Taxonomy
Reference
1
Authors
Agner, K.
Title
Myeloperoxidase.
Journal
Adv Enzymol 3:137-148 (1943)
Reference
Authors
Harrison JE, Schultz J
Title
Studies on the chlorinating activity of myeloperoxidase.
Journal
J Biol Chem 251:1371-4 (1976)
Reference
Authors
Furtmuller PG, Burner U, Obinger C
Title
Reaction of myeloperoxidase compound I with chloride, bromide, iodide, and thiocyanate.
Journal
Reference
Authors
Tuynman A, Spelberg JL, Kooter IM, Schoemaker HE, Wever R
Title
Enantioselective epoxidation and carbon-carbon bond cleavage catalyzed by Coprinus cinereus peroxidase and myeloperoxidase.
Journal
Reference
Authors
Klebanoff SJ
Title
Myeloperoxidase: friend and foe.
Journal
Reference
Authors
Fiedler TJ, Davey CA, Fenna RE
Title
X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution.
Journal
Sequence
Reference
Authors
Gaut JP, Yeh GC, Tran HD, Byun J, Henderson JP, Richter GM, Brennan ML, Lusis AJ, Belaaouaj A, Hotchkiss RS, Heinecke JW
Title
Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.11.2.2
ExPASy - ENZYME nomenclature database: 1.11.2.2